The specific androgen-binding cytosol receptor has been partially purified from the crude 8S cytosol fraction. It sediments as a 7.6S androgen-binding peak by glycerol gradient centrifugation, translocates its bound androgens target tissue-specifically into prostate nuclus, and is capable of stimulating transcription of DNA in vitro. Interaction of (3H)DHT-4S cytosol fraction with 8S cytosol fraction results innthe formation of the specific androgen-binding receptor, and this interaction is temperature-dependent. The soluble androgen nuclear acceptor has been partially purified from 0.35 M NaCl extract of rat prostate nuclei. The soluble acceptor activity is stimulated by native DNA. It binds non-specifically to E. coli and prostate DNA and stimulates RNA synthesis in vitro. In vitro interaction of (3H) DHT-receptor with prostate chromatin reveals multiple androgen-binding sites in the target cell chromatin. One of the chromatin fractions, the residual fraction that is unextractable by 2 M NaC1, is especially active in binding to (3H)DHT-receptor. The dependence of the prostate chromtin on the residual fraction for tissue-specific translocation of and interaction with (3H)DHT-receptor suggests an acceptor role for the residual fraction in androgen action.